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  • Title: Rodent tissue alpha-L-fucosidases: analysis of brain and spleen isoforms and characterization of the purified hamster liver enzyme.
    Author: Shoarinejad F, Alhadeff JA.
    Journal: Comp Biochem Physiol B; 1993; 105(3-4):523-8. PubMed ID: 8365108.
    Abstract:
    1. Isoelectric focusing of brain and spleen alpha-L-fucosidases from four rodents (rat, mouse, guinea-pig, hamster) indicated that only mouse and hamster tissues contained isoforms with significant amounts of activity above pI 7.0. 2. Hamster liver alpha-L-fucosidase was purified approximately 57,000-fold in 80% yield (to a final specific activity of 24,700 nmol/min/mg protein) by affinity chromatography on agarose-epsilon-aminocaproyl-fucosamine. 3. SDS-PAGE analysis of hamster liver alpha-L-fucosidase indicated the presence of one to two closely-spaced subunits at 56 and 60 kDa. Western blotting analysis indicated the hamster enzyme was recognized by polyclonal antibodies but not by a monoclonal antibody (both antibodies prepared against human liver alpha-L-fucosidase). 4. The pH-activity curve of hamster liver alpha-L-fucosidase is broad with an optimum centered around pH 6.8 and with high activity between pH 5.5 and 7.5.
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